Journal
SCIENCE
Volume 320, Issue 5874, Pages 376-379Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1154994
Keywords
-
Categories
Ask authors/readers for more resources
Type 1 pili from uropathogenic Escherichia coli are a prototype of adhesive surface organelles assembled and secreted by the conserved chaperone/ usher pathway. We reconstituted type 1 pilus biogenesis from purified pilus proteins. The usher FimD acted as a catalyst to accelerate the ordered assembly of protein subunits independently of cellular energy. Its activity was highly dependent on the adhesin subunit FimH, which triggered the conversion of FimD into a high-efficiency assembly catalyst. Furthermore, a simple kinetic model adequately rationalized usher- catalyzed pilus assembly in vivo. Our results contribute to a mechanistic understanding of protein- catalyzed biogenesis of supramolecular protein complexes at the bacterial outer cell membrane.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available